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Mills, Jeffrey L.; Szyperski, Thomas, E-mail: szypersk@chem.buffalo.edu2002
AbstractAbstract
[en] The impact of studying protein dynamics in supercooled water for identifying slow motional modes on the μs time scale is demonstrated. Backbone 15N spin relaxation parameters were measured at -13 deg. C for ubiquitin, which plays a central role for signaling proteolysis, cellular trafficking and kinase activation in eukaryotic organisms. A hitherto undetected motional mode involving Val 70 was found, which may well play an important role for ubiquitin recognition. The measurement of rotating frame 15N relaxation times as a function of the spin-lock field allowed determination of the correlation time of this motional mode, which would not have been feasible above 0 deg. C
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Copyright (c) 2002 Kluwer Academic Publishers; Country of input: International Atomic Energy Agency (IAEA)
Record Type
Journal Article
Journal
Journal of Biomolecular NMR; ISSN 0925-2738;
; v. 23(1); p. 63-67

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